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Literature summary for 4.2.99.18 extracted from

  • Kanazhevskaya, L.Y.; Koval, V.V.; Zharkov, D.O.; Strauss, P.R.; Fedorova, O.S.
    Conformational transitions in human AP endonuclease 1 and its active site mutant during abasic site repair (2010), Biochemistry, 49, 6451-6461.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

Protein Variants

Protein Variants Comment Organism
Y171F/P173L/N174K mutation results in 20000fold decrease in the reaction rate and reduced binding affinity Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.000093
-
12-mer oligodeoxyribonucleotide containing a natural AP site wild-type, pH 7.5, 25°C Homo sapiens
0.000098
-
12-mer oligodeoxyribonucleotide containing a tetrahydrofuran analogue at the natural AP site wild-type, pH 7.5, 25°C Homo sapiens
0.00022
-
12-mer oligodeoxyribonucleotide containing a natural AP site mutant Y171F/P173L/N174K, pH 7.5, 25°C Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
12-mer oligodeoxyribonucleotide containing a 2'-deoxyguanosine at the natural AP site
-
Homo sapiens ?
-
?
12-mer oligodeoxyribonucleotide containing a natural AP site the minimal kinetic model for the natural AP site incision consists of four stages corresponding to three different transient states of APE1. When the enzyme is complexed with the AP-substrate, the catalytic cycle is completed within 3 s Homo sapiens ?
-
?
12-mer oligodeoxyribonucleotide containing a tetrahydrofuran analogue at the natural AP site
-
Homo sapiens ?
-
?
additional information wild-type APE1 undergoes at least four conformational transitions during the processing of abasic sites in DNA. Nonspecific interactions of APE1 with undamaged DNA can be described by a two-step kinetic scheme. APE1 molecule undergoes at least four conformational transitions, including nonspecific encounter complex formation, mutual adjustment of the enzyme and DNA substrate structures for catalysis, catalytic incision of the substrate, and release of the enzyme from its complex with the product. The C1'-hydroxyl moiety of the abasic site is required for the most effective recognition and catalysis Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
AP endonuclease 1
-
Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.000153
-
12-mer oligodeoxyribonucleotide containing a natural AP site mutant Y171F/P173L/N174K, pH 7.5, 25°C Homo sapiens
1
-
12-mer oligodeoxyribonucleotide containing a tetrahydrofuran analogue at the natural AP site wild-type, pH 7.5, 25°C Homo sapiens
2.8
-
12-mer oligodeoxyribonucleotide containing a natural AP site wild-type, pH 7.5, 25°C Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.63
-
12-mer oligodeoxyribonucleotide containing a natural AP site mutant Y171F/P173L/N174K, pH 7.5, 25°C Homo sapiens
10000
-
12-mer oligodeoxyribonucleotide containing a tetrahydrofuran analogue at the natural AP site wild-type, pH 7.5, 25°C Homo sapiens
30000
-
12-mer oligodeoxyribonucleotide containing a natural AP site wild-type, pH 7.5, 25°C Homo sapiens